5JVO
Crystal structure of the Arginine Repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis
5JVO の概要
| エントリーDOI | 10.2210/pdb5jvo/pdb |
| 分子名称 | Arginine repressor, TYROSINE, SULFATE ION, ... (4 entities in total) |
| 機能のキーワード | arginine repressor, dna binding protein |
| 由来する生物種 | Corynebacterium pseudotuberculosis |
| 細胞内の位置 | Cytoplasm : A0A0E3UAP8 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 21726.26 |
| 構造登録者 | Mariutti, R.B.,Ullah, A.,Murakami, M.T.,Arni, R.K. (登録日: 2016-05-11, 公開日: 2016-08-31, 最終更新日: 2023-09-27) |
| 主引用文献 | Mariutti, R.B.,Ullah, A.,Araujo, G.C.,Murakami, M.T.,Arni, R.K. Tyrosine binding and promiscuity in the arginine repressor from the pathogenic bacterium Corynebacterium pseudotuberculosis. Biochem.Biophys.Res.Commun., 475:350-355, 2016 Cited by PubMed Abstract: The arginine repressor (ArgR) regulates arginine biosynthesis in a number of microorganisms and consists of two domains interlinked by a short peptide; the N-terminal domain is involved in DNA binding and the C-terminal domain binds arginine and forms a hexamer made-up of a dimer of trimers. The crystal structure of the C-terminal domain of ArgR from the pathogenic Corynebacterium pseudotuberculosis determined at 1.9 Å resolution contains a tightly bound tyrosine at the arginine-binding site indicating hitherto unobserved promiscuity. Structural analysis of the binding pocket displays clear molecular adaptations to accommodate tyrosine binding suggesting the possible existence of an alternative regulatory process in this pathogenic bacterium. PubMed: 27233609DOI: 10.1016/j.bbrc.2016.05.091 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






